ID F8E088_CORRG Unreviewed; 584 AA.
AC F8E088;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|ARBA:ARBA00018893, ECO:0000256|HAMAP-Rule:MF_00377};
GN Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN ECO:0000313|EMBL:AEI08364.1};
GN OrderedLocusNames=CRES_0001 {ECO:0000313|EMBL:AEI08364.1};
OS Corynebacterium resistens (strain DSM 45100 / JCM 12819 / GTC 2026 / SICGH
OS 158).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=662755 {ECO:0000313|EMBL:AEI08364.1, ECO:0000313|Proteomes:UP000000492};
RN [1] {ECO:0000313|EMBL:AEI08364.1, ECO:0000313|Proteomes:UP000000492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45100 / JCM 12819 / GTC 2026 / SICGH 158
RC {ECO:0000313|Proteomes:UP000000492};
RX PubMed=22524407; DOI=10.1186/1471-2164-13-141;
RA Schroder J., Maus I., Meyer K., Wordemann S., Blom J., Jaenicke S.,
RA Schneider J., Trost E., Tauch A.;
RT "Complete genome sequence, lifestyle, and multi-drug resistance of the
RT human pathogen Corynebacterium resistens DSM 45100 isolated from blood
RT samples of a leukemia patient.";
RL BMC Genomics 13:141-141(2012).
CC -!- FUNCTION: Plays an important role in the initiation and regulation of
CC chromosomal replication. Binds to the origin of replication; it binds
CC specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-
CC TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
CC {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00377}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|ARBA:ARBA00006583,
CC ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU004227}.
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DR EMBL; CP002857; AEI08364.1; -; Genomic_DNA.
DR AlphaFoldDB; F8E088; -.
DR STRING; 662755.CRES_0001; -.
DR KEGG; crd:CRES_0001; -.
DR eggNOG; COG0593; Bacteria.
DR HOGENOM; CLU_026910_2_0_11; -.
DR Proteomes; UP000000492; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR CDD; cd06571; Bac_DnaA_C; 1.
DR Gene3D; 1.10.1750.10; -; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00377; DnaA_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR001957; Chromosome_initiator_DnaA.
DR InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR InterPro; IPR018312; Chromosome_initiator_DnaA_CS.
DR InterPro; IPR013317; DnaA.
DR InterPro; IPR013159; DnaA_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010921; Trp_repressor/repl_initiator.
DR NCBIfam; TIGR00362; DnaA; 1.
DR PANTHER; PTHR30050; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1.
DR PANTHER; PTHR30050:SF2; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1.
DR Pfam; PF00308; Bac_DnaA; 1.
DR Pfam; PF08299; Bac_DnaA_C; 1.
DR PRINTS; PR00051; DNAA.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00760; Bac_DnaA_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48295; TrpR-like; 1.
DR PROSITE; PS01008; DNAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00377};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00377};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00377};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00377};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00377}; Reference proteome {ECO:0000313|Proteomes:UP000000492}.
FT DOMAIN 278..486
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 488..557
FT /note="Chromosomal replication initiator DnaA C-terminal"
FT /evidence="ECO:0000259|SMART:SM00760"
FT REGION 51..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 286..293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ SEQUENCE 584 AA; 65532 MW; A8FB691EA2413F2D CRC64;
MLLQITPVTL IGNIAVLQTP SKWIKEEVER ELTQPIKDVL ASRLQINTTL AISSRDDGNS
SNTGENRHND TEHTLNEQHS SPHDYTTDPK SQHESQSGNS NQAQPGYQQP STGPQNEDPF
GHAGNDSNSA SEQHSRKNSN GRTNQNNRLT NNDFGDYERN GFPDYGDRKA SSLKGQRPRR
EQNNEAFSLD EWVDLKEPEA EAAAIANTKK RNELLRQNGI EPLARPGMSP AGNQSAGKET
ESETLLNKNY TFETFVIGSS NNFANAACRA VAESPAKAYN PLFIWGESGL GKTHLLHAIG
HYAKELRPNM RVRYVSSEEL TNDFINSIAT DTREAFKRRY RNVDMLIVDD IQFLEGKEST
QEEFFHTFNA LHQANKQIVL SSDRPPKKLT TLEDRLRTRF EGGLTTDVTS PDLETRIAIL
SKKAQLEGIQ LPEDVKQLIA NRYDTSIRVL EGALIRVIAY CSLGDEPISL EAAEVALRDI
NNGTVEVTPQ AVIEVVAHYF NLTTDELVGK GRSRRFVQAR QIAMYLCREL TDLSLPKLGA
AFGGRDHTTV MYAERRIRES LTENKKVFDQ VQELTQKIEN HARN
//
